3azd

Crystal structure of tropomyosin N-terminal fragment at 0.98A resolution

Method: X-RAY DIFFRACTION Dmax: 49.9 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

short alpha-tropomyosin,transcription factor GCN4

OrganismNot specified

UniProt P03069

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 264–281 Chain B; UniProt 264–281 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.17M ammonium sulfate, 10% PEG 4000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 0.98 Å R-free 0.171

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

162 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–37; UniProt 264–281 Author chain B; PDBConstruct 20–37; UniProt 264–281

short alpha-tropomyosin,transcription factor GCN4

OrganismNot specified

UniProt Q6AZ25

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–20 Chain B; UniProt 2–20 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.17M ammonium sulfate, 10% PEG 4000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 0.98 Å R-free 0.171

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q6AZ25_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–19; UniProt 2–20 Author chain B; PDBConstruct 1–19; UniProt 2–20

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 3azd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3azd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3azd
Deposition date deposition_date2011-05-23
Structure title titleCrystal structure of tropomyosin N-terminal fragment at 0.98A resolution
Keywords keywordscoiled-coil, actin-binding protein, muscle protein; ACTIN-BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.16
Radius of gyration Rg (electron density) rg_electron13.66
Forward intensity I(0) i01179410.00
Molecular weight molecular_weight7154.0 kDa
Excluded volume excluded_volume9013 ų
Envelope volume envelope_volume11189 ų
Hydration-shell volume shell_volume7740 ų
Envelope diameter envelope_diameter47.5
Shell Rg shell_rg17.73
Envelope Rg envelope_rg14.31
Shape Rg shape_rg13.59
Total Rg total_rg14.89
Total atoms total_atoms504
Residues n_residues60
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax49.9
Rg (real space) rg_real14.28
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.1790e+06
I(0) uncertainty (real space) i0_real_error1.4320e+04
Rg (reciprocal space) rg_reciprocal14.27
I(0) (reciprocal space) i0_reciprocal1179000.0000
Solution quality estimate total_estimate0.8404
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.5
Skewness Skewness skewness0.543
Kurtosis Kurtosis kurtosis-0.043
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha183900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.763; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)